Lipopolysaccharide- and β-1,3-glucan-binding protein from Fenneropenaeus merguiensis functions as a pattern recognition receptor with a broad specificity for diverse pathogens in the defense against microorganisms

• Published in: Developmental and comparative immunology Vol. 67; pp. 434 - 444
• Main Authors: Chaosomboon, Areerat, Phupet, Benjaporn, Rattanaporn, Onnicha, Runsaeng, Phanthipha, Utarabhand, Prapaporn
• Format: Journal Article
• Language: English
• Published: United States Elsevier Ltd 01.02.2017; Elsevier Science Ltd
• Subjects: Agglutination; Amino acid sequence; Amino acids; Animals; Bacteria; beta-Glucans - metabolism; Cells, Cultured; Cloning, Molecular; Crustaceans; Enzyme-linked immunosorbent assay; Fenneropenaeus merguiensis; Glucan; Gram-positive bacteria; Hepatopancreas; Hepatopancreas - metabolism; Immune response; Immune system; Immunity; Immunity, Innate; Innate immunity; Lectins - genetics; Lipopolysaccharide- and β-1,3-glucan-binding protein (LGBP); Lipopolysaccharides; Lipopolysaccharides - metabolism; Lipopolysaccharides - pharmacology; Lipoteichoic acid; Microorganisms; mRNA; Pathogen-Associated Molecular Pattern Molecules - immunology; Pathogens; Pattern recognition; Pattern recognition receptors; Penaeidae - immunology; Phosphorylation; Polysaccharides; Protein Binding; Proteins; Receptors, Pattern Recognition - genetics; Receptors, Pattern Recognition - metabolism; Saccharides; Teichoic Acids - pharmacology; Up-Regulation; Vibrio - immunology; Vibrio harveyi; Vibrio Infections - immunology; Waterborne diseases; Western blotting; Yeast; Lipopolysaccharide- and β-1,3-glucan-binding protein (LGBP); Fenneropenaeus merguiensis; Immune response; Vibrio harveyi; Hepatopancreas
• ISSN: 0145-305X; 1879-0089
• DOI: 10.1016/j.dci.2016.07.006

In crustaceans, lipopolysaccharide- and β-1,3-glucan-binding protein (LGBP) plays an important role in innate immunity by mediating the recognition of pathogens to host cells. Hereby, LGBP was cloned from Fenneropenaeus merguiensis hepatopancreas. Its full-length cDNA (1280 bp) had an open reading frame of 1101 bp, encoding a peptide of 366 amino acids. The LGBP primary structure comprises a recognition motif for β-1,3-linkage of polysaccharides, two integrin binding motifs, a kinase C phosphorylation site and a bacterial glucanase motif. The LGBP mRNA was strongly expressed in hepatopancreas and significantly up-regulated to get the maximum at 12 h upon Vibrio harveyi challenge. Recombinant LGBP (rLGBP) could agglutinate Gram-negative and Gram-positive bacteria including yeast with Ca2+-dependence. V. harveyi agglutination induced by rLGBP was intensively inhibited by lipoteichoic acid, less in order were lipopolysaccharide, β-1,3-glucan and N-acetyl neuraminic acid. Western blotting revealed that rLGBP bound widely to Gram-negative and Gram-positive bacteria and also yeast. By ELISA quantification, rLGBP could bind to β-1,3-glucan better than to lipopolysaccharide and lipoteichoic acid. These findings suggest that LGBP may function as a receptor which recognizes invading diverse pathogens and contribute in F. merguiensis immune response. •FmLGBP was cloned from Fenneropenaeus merguiensis hepatopancreas containing LGBP domains.•LGBP mRNA expression was up-regulated upon challenge with pathogenic Vibrio harveyi.•rLGBP could agglutinate and bind Gram-negative and Gram-positive bacteria and yeast.•FmLGBP may serve as receptor molecules to recognize invading diverse microorganisms.•FmLGBP may act as PRP in the innate immune response in this species of shrimp.